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Neurosci Lett. 2003 May 22;342(3):151-4.
Immunohistochemical study on the distribution of alpha-synuclein in the central nervous system of transgenic mice expressing a human Cu/Zn superoxide dismutase mutation.

Chung YH, Joo KM, Kim MJ, Cha CI.

Department of Anatomy, Seoul National University College of Medicine, 28 Yongon-Dong, Chongno-Gu, Seoul 110-799, South Korea.

We used the SOD1(G93A) transgenic mice as an in vivo model of amyotrophic lateral sclerosis (ALS) and performed immunohistochemical studies to investigate whether alpha-synuclein is involved in the pathogenesis of ALS. In the spinal cord of transgenic mice, immunohistochemistry showed intense staining of alpha-synuclein mainly in the anterior horn. In the hippocampus of transgenic mice, differential increases in the staining density of alpha-synuclein were observed. In the cerebellar cortex of transgenic mice, the prominent immunostaining of alpha-synuclein was found in the molecular and granular layers. The present study provides the first in vivo evidence that alpha-synuclein immunoreactivity was increased in the central nervous system of SOD(G93A) transgenic mice, suggesting that alpha-synuclein might play an important role in the pathogenesis of ALS. However, the functional implications of these increases require elucidation.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12757887&dopt=Abstract

Neurosci Lett. 2003 May 22;342(3):175-8.
Novel variants of murine serotonin transporter mRNA and the promoter activity of its upstream site.

Sakai K, Hasegawa C, Okura M, Morikawa O, Ueyama T, Shirai Y, Sakai N, Saito N.

Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, 1-1, Rokko-dai, Nada, 657-8501, Kobe, Japan. naosaitobe-u.ac.jp

Three variants of murine serotonin transporter (5-HTT) mRNA, which consist of a different exon-one (exon 1a, exon 1b or exon 1c) and the same exon-two to exon-five, were identified. The promoter region for each exon 1 (p1a, p1b and p1c, respectively), ligated to pGL-3 enhancer vector, had activities significantly higher than the empty vector in all cell lines tested except p1c in PC-12, whereas the activity of p1c was significantly lower than the others. Effects of the treatment of dibutyryl-cyclic AMP, human interferon-alpha or mouse interferon-gamma have different profiles among COS-7, PC-12, C6 glioma and immortalized rat serotonergic raphe neurons, RN46A. These three promoter regions may play a role in the transcription of the 5-HTT and could offer a model of the regulation of 5-HTT production in humans and further the pathogenesis of depression.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12757893&dopt=Abstract

Biochim Biophys Acta. 2003 May 20;1638(1):43-9.
Functional analysis of PCCB mutations causing propionic acidemia based on expression studies in deficient human skin fibroblasts.

Perez-Cerda C, Clavero S, Perez B, Rodriguez-Pombo P, Desviat LR, Ugarte M.

Dpto. de Biologia Molecular, Centro de Biologia Molecular Severo Ochoa, Universidad Autonoma de Madrid, Cantoblanco, 28049, Madrid, Spain.

Propionic acidemia (PA) is a recessive disorder caused by a deficiency of propionyl-CoA carboxylase (PCC), a dodecameric enzyme composed of two different proteins alpha-PCC and beta-PCC, nuclear encoded by the PCCA and PCCB genes, respectively. Mutations in either gene cause PA and to date, up to 47 different allelic variations in the PCCB gene have been identified in different populations. In this work, we describe the expression studies of 18 PCCB sequence changes in order to elucidate their functional consequences. We have used a PCCB-deficient transformed fibroblast cell line to target the wild-type and mutant proteins to their physiological situation, analysing the effect of the mutations on PCC activity and protein stability. Of the 18 mutant proteins tested for activity, those carrying the L17M and A497V substitutions showed an activity similar to the wild-type one, which proves that these changes do not have any effect on protein activity. The other 16 mutant proteins exhibited two different functional behaviours, 3 retained substantial activity (K218R, R410W and N536D), and the remaining 13 proteins showed null or very low activity. Western blot analysis demonstrated instability only for the L519P, R512C and G112D mutant proteins. We have proved the pathogenicity of R67S, R165Q and G112D mutation in PCCB gene, expressed for the first time in this work. The information derived from the expression analysis is discussed in the phenotype and genotype context in order to improve the knowledge of this complex disease.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12757933&dopt=Abstract

Biochim Biophys Acta. 2003 May 20;1638(1):57-62.
Extracellular matrix and nuclear abnormalities in skeletal muscle of a patient with Walker-Warburg syndrome caused by POMT1 mutation.

Sabatelli P, Columbaro M, Mura I, Capanni C, Lattanzi G, Maraldi NM, Beltran-Valero de Barnabe D, van Bokoven H, Squarzoni S, Merlini L.

Istituto per i Trapianti d'organo e l'Immunocitologia (ITOI) CNR, c/o IOR, Bologna, Italy.

Walker-Warburg syndrome (WWS) is an autosomal recessive disorder characterized by congenital muscular dystrophy, structural eye abnormalities and severe brain malformations. We performed an immunohistochemical and electron microscopy study of a muscle biopsy from a patient affected by WWS carrying a homozygous frameshift mutation in O-mannosyltransferase 1 gene (POMT1). alpha-Dystroglycan glycosylated epitope was not detected in muscle fibers and intramuscular peripheral nerves. Laminin alpha2 chain and perlecan were reduced in muscle fibers and well preserved in intramuscular peripheral nerves. The basal lamina in several muscle fibers showed discontinuities and detachment from the plasmalemma. Most nuclei, including myonuclei and satellite cell nuclei, showed detachment or complete absence of peripheral heterochromatin from the nuclear envelope. Apoptotic changes were detected in 3% of muscle fibers. The particular combination of basal lamina and nuclear changes may suggest that a complex pathogenetic mechanism, affecting several subcellular compartments, underlies the degenerative process in WWS muscle.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12757935&dopt=Abstract

FEMS Microbiol Lett. 2003 May 16;222(1):39-43.
Involvement of enterobactin in norepinephrine-mediated iron supply from transferrin to enterohaemorrhagic Escherichia coli.

Freestone PP, Haigh RD, Williams PH, Lyte M.

Department of Microbiology and Immunology, University of Leicester, Leicester, UK.

Exposure of bacteria to members of the stress-associated family of catecholamine hormones, principally norepinephrine, has been demonstrated to increase both growth and production of virulence-related factors. Mutation of genes for enterobactin synthesis and uptake revealed an absolute requirement for enterobactin in norepinephrine-stimulated growth of Escherichia coli O157:H7. The autoinducer produced by norepinephrine-stimulated E. coli could not substitute for enterobactin. We also demonstrate that norepinephrine promotes iron shuttling between transferrin molecules, thereby enabling the bacterial siderophore enterobactin to more readily acquire iron for growth. These results suggest one of the possible mechanisms by which the hormonal output of stress may affect enterohaemorrhagic E. coli pathogenicity.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12757944&dopt=Abstract

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